Femtosecond laser pulses at 270nm, the Ti:Sapph 3rd harmonic, are utilized to break the S-S bond in small helix bundles that are constrained to be nonhelical as a result of the disulfide bridge. The resulting processes involve helix formation and geminate recombination of the sulfhydryl radicals. Both are interesting since they are controlled by the fluctuations of the protein atoms. This project involves quite the new technology of ultraviolet pumping and infrared probing of protein dynamics [See Highlights for update]. A major technical goal of this work is to control the excitation processes that occur when water (or D2O) are irradiated with intense UV pulses. The two photon absorption leads to the efficient formation of solvated electrons which interfere with the methods of probing structure changes in the visible and near IR. Preliminary results for these peptides are now in place (see Highlights).